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Title: Specific fixation of bovine brain and retinal acidic and basic fibroblast growth factors to mouse embryonic eye basement membranes

Abstract

The labeling pattern of mouse embryonic eye frozen sections incubated with radioiodinated brain acidic and basic fibroblasts growth factors (aFGF and bFGF) was investigated by autoradiography. Both growth factors bind to basement membranes in a dose-dependent way, with a higher affinity for bFGF. Similar data were obtained with eye-derived growth factors (EDGF), the retinal forms of FGF. There was a heterogeneity in the affinity of the various basement membranes toward these growth factors. The specificity of the growth factor-basement membrane interaction was demonstrated by the following experiments: (i) an excess of unlabeled growth factor displaced the labeling; (ii) unrelated proteins with different isoelectric points did not modify the labeling; and (iii) iodinated EGF or PDGF did not label basement membrane. In order to get a better understanding of the nature of this binding, the authors performed the incubation of the frozen sections with iodinated FGFs preincubated with various compounds. These results demonstrate that FGFs bind specifically to basement membranes, probably on the polysaccharidic part of the proteoheparan sulfate, and suggest that this type of interaction may be a general feature of the mechanism of action of these growth factors.

Authors:
; ;  [1]; ; ;  [2]
  1. (INSERM U.118, Paris (France))
  2. (Universite Paris Val de Marne, Creteil (France))
Publication Date:
OSTI Identifier:
6531637
Resource Type:
Journal Article
Resource Relation:
Journal Name: Experimental Cell Research; (USA); Journal Volume: 171:1
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; FETAL MEMBRANES; CROSS-LINKING; GROWTH FACTORS; RADIORECEPTOR ASSAY; POLYPEPTIDES; BRAIN; CATTLE; ELECTROPHORESIS; EMBRYOS; EYES; FIBROBLASTS; IODINE 125; MICE; RETINA; SODIUM IODIDES; ALKALI METAL COMPOUNDS; ANIMAL CELLS; ANIMALS; BETA DECAY RADIOISOTOPES; BODY; BODY AREAS; CENTRAL NERVOUS SYSTEM; CHEMICAL REACTIONS; CONNECTIVE TISSUE CELLS; DAYS LIVING RADIOISOTOPES; DOMESTIC ANIMALS; ELECTRON CAPTURE RADIOISOTOPES; FACE; HALIDES; HALOGEN COMPOUNDS; HEAD; INORGANIC PHOSPHORS; INTERMEDIATE MASS NUCLEI; IODIDES; IODINE COMPOUNDS; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; MAMMALS; MEMBRANES; MITOGENS; NERVOUS SYSTEM; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; ORGANS; PEPTIDES; PHOSPHORS; POLYMERIZATION; PROTEINS; RADIOISOTOPES; RODENTS; RUMINANTS; SENSE ORGANS; SODIUM COMPOUNDS; SOMATIC CELLS; TRACER TECHNIQUES; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Jeanny, J.C., Fayein, N., Courtois, Y., Moenner, M., Chevallier, B., and Barritault, D. Specific fixation of bovine brain and retinal acidic and basic fibroblast growth factors to mouse embryonic eye basement membranes. United States: N. p., 1987. Web. doi:10.1016/0014-4827(87)90251-5.
Jeanny, J.C., Fayein, N., Courtois, Y., Moenner, M., Chevallier, B., & Barritault, D. Specific fixation of bovine brain and retinal acidic and basic fibroblast growth factors to mouse embryonic eye basement membranes. United States. doi:10.1016/0014-4827(87)90251-5.
Jeanny, J.C., Fayein, N., Courtois, Y., Moenner, M., Chevallier, B., and Barritault, D. 1987. "Specific fixation of bovine brain and retinal acidic and basic fibroblast growth factors to mouse embryonic eye basement membranes". United States. doi:10.1016/0014-4827(87)90251-5.
@article{osti_6531637,
title = {Specific fixation of bovine brain and retinal acidic and basic fibroblast growth factors to mouse embryonic eye basement membranes},
author = {Jeanny, J.C. and Fayein, N. and Courtois, Y. and Moenner, M. and Chevallier, B. and Barritault, D.},
abstractNote = {The labeling pattern of mouse embryonic eye frozen sections incubated with radioiodinated brain acidic and basic fibroblasts growth factors (aFGF and bFGF) was investigated by autoradiography. Both growth factors bind to basement membranes in a dose-dependent way, with a higher affinity for bFGF. Similar data were obtained with eye-derived growth factors (EDGF), the retinal forms of FGF. There was a heterogeneity in the affinity of the various basement membranes toward these growth factors. The specificity of the growth factor-basement membrane interaction was demonstrated by the following experiments: (i) an excess of unlabeled growth factor displaced the labeling; (ii) unrelated proteins with different isoelectric points did not modify the labeling; and (iii) iodinated EGF or PDGF did not label basement membrane. In order to get a better understanding of the nature of this binding, the authors performed the incubation of the frozen sections with iodinated FGFs preincubated with various compounds. These results demonstrate that FGFs bind specifically to basement membranes, probably on the polysaccharidic part of the proteoheparan sulfate, and suggest that this type of interaction may be a general feature of the mechanism of action of these growth factors.},
doi = {10.1016/0014-4827(87)90251-5},
journal = {Experimental Cell Research; (USA)},
number = ,
volume = 171:1,
place = {United States},
year = 1987,
month = 7
}
  • Nerve growth factor (NGF) and acidic or basic fibroblast growth factor (aFGF and bFGF, respectively) induce neurite outgrowth from the rat pheochromocytoma cell line, PC12. The neurites induced by these three factors are stable for up to a month in cell culture in the continued presence of any of the above growth factors. bFGF (ED50 = 30 pg/ml) is 800 fold more potent in stimulating neurite outgrowth than aFGF (ED50 = 25 ng/ml) and 260 fold more potent than NGF (ED50 = 8 ng/ml). While the neurotropic activities of aFGF and NGF are potentiated by heparin, that of bFGF ismore » both partially inhibited or stimulated, depending upon the concentration of bFGF. Radioreceptor binding experiments show that aFGF and bFGF bind to a common binding site on the PC12 cell surface. Affinity labeling studies demonstrate a single receptor with an apparent molecular weight of 145,000 daltons, which corresponds to the high molecular weight receptor identified in BHK-21 cells. NGF does not appear to compete with aFGF or bFGF for binding to the receptor. Heparin blocked the binding of bFGF to the receptor but had only a small inhibitory effect on the binding of aFGF to the receptor. Thus, it appears that heparin inhibition of the neurotropic effects of bFGF occurs, at least in part, by impairing the interaction of bFGF with the receptor, while having little effect on that of aFGF. The stimulatory effects of heparin on the neurotropic activity of aFGF, bFGF, and NGF may occur through a site not associated with the respective cellular receptor for the growth factors.« less
  • The growth autonomy of human tumor cells is considered due to the endogenous production of growth factors. Transcriptional expression of candidates for autocrine stimulatory factors such as basic fibroblast growth factor (FGF), acidic FGF, and transforming growth factor type {beta} were determined in human brain tumors. Basic FGF was expressed abundantly in 17 of 18 gliomas, 20 of 22 meningiomas, and 0 of 5 metastatic brain tumors. The level of mRNA expression of acidic FGF in gliomas was significant. In contrast, transforming growth factor type {beta}1 was expressed in all the samples investigated. The mRNA for basic FGF and itsmore » peptide were localized in tumor cells in vivo by in situ hybridization and immunohistochemistry, showing that basic FGF is actually produced in tumor cells. The results suggest that tumor-derived basic FGF is involved in the progression of gliomas and meningiomas in vivo, whereas acidic FGF is expressed in a tumor origin-specific manner, suggesting that acidic FGF works in tandem with basic FGF in glioma tumorigenesis.« less
  • A M/sub r/ 25,000 form of basic fibroblast growth factor (bFGF) has been isolated from guinea pig grain along with the typical M/sub r/ 18,000 form. Both forms were purified to homogeneity by a combination of heparin-affinity chromatography and ion-exchange chromatography on an FPLC Mono S column. The M/sub r/ 25,000 form, like the M/sub r/ 18,000 form was not eluted from the heparin-affinity column with 0.95 M NaCl, but was eluted with 2 M NaCl. The M/sub r/ 25,000 guinea pig protein stimulated plasminogen activator production by cultured bovine capillary endothelial cells in a dose-dependent manner at concentration ofmore » 0.1-10 ngml, the same range that was effective for guinea pig and human M/sub r/ 18,000 bFGFs. The binding of human /sup 125/I-labeled bFGF to baby hamster kidney cells is inhibited equally by the M/sub r/ 25,000 guinea pig protein and the M/sub r/ 18,000 guinea pig and human bFGFs. Polyclonal antibodies raised against human bFGF recognize both the M/sub r/ 25,000 and 18,000 guinea pig proteins in an immunoblot analysis. In a radioimmunoassay, both the M/sub r/ 25,000 and M/sub r/ 18,000 guinea pig proteins compete equally well with iodinated human bFGF for binding to the anti-human bFGF antibodies. When treated with low concentrations of trypsin, the M/sub r/ 25,000 guinea pig bFGF was converted to a M/sub r/ 18,000 protein. These results show that the two molecules are closely related and suggest that the M/sub r/ 25,000 protein shares substantial homology with the M/sub r/ 18,000 bFGF« less
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